DHH1_YEAST
ID DHH1_YEAST Reviewed; 506 AA.
AC P39517; D6VRJ0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=ATP-dependent RNA helicase DHH1 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE AltName: Full=DExD/H-box helicase 1 {ECO:0000303|PubMed:8511971};
GN Name=DHH1 {ECO:0000303|PubMed:8511971};
GN OrderedLocusNames=YDL160C {ECO:0000312|SGD:S000002319};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8511971; DOI=10.1002/yea.320090414;
RA Strahl-Bolsinger S., Tanner W.;
RT "A yeast gene encoding a putative RNA helicase of the 'DEAD'-box family.";
RL Yeast 9:429-432(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH POP2, AND ASSOCIATION WITH THE CCR4-NOT COMPLEX.
RX PubMed=9504907; DOI=10.1093/genetics/148.2.571;
RA Hata H., Mitsui H., Liu H., Bai Y., Denis C.L., Shimizu Y., Sakai A.;
RT "Dhh1p, a putative RNA helicase, associates with the general transcription
RT factors Pop2p and Ccr4p from Saccharomyces cerevisiae.";
RL Genetics 148:571-579(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH DCP1; LSM1; PAT1 AND POP2.
RX PubMed=11780629; DOI=10.1017/s135583820101994x;
RA Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R.;
RT "The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts
RT with both the decapping and deadenylase complexes.";
RL RNA 7:1717-1727(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KEM1 AND PAT1.
RX PubMed=12032091; DOI=10.1093/emboj/21.11.2788;
RA Fischer N., Weis K.;
RT "The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1.";
RL EMBO J. 21:2788-2797(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH CDC39.
RX PubMed=11696541; DOI=10.1074/jbc.m107979200;
RA Maillet L., Collart M.A.;
RT "Interaction between Not1p, a component of the Ccr4-not complex, a global
RT regulator of transcription, and Dhh1p, a putative RNA helicase.";
RL J. Biol. Chem. 277:2835-2842(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH LARGE COMPLEXES.
RX PubMed=12930949; DOI=10.1093/nar/gkg712;
RA Tseng-Rogenski S.S.-I., Chong J.-L., Thomas C.B., Enomoto S., Berman J.,
RA Chang T.-H.;
RT "Functional conservation of Dhh1p, a cytoplasmic DExD/H-box protein present
RT in large complexes.";
RL Nucleic Acids Res. 31:4995-5002(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12730603; DOI=10.1126/science.1082320;
RA Sheth U., Parker R.;
RT "Decapping and decay of messenger RNA occur in cytoplasmic processing
RT bodies.";
RL Science 300:805-808(2003).
RN [12]
RP FUNCTION.
RX PubMed=15166134; DOI=10.1534/genetics.167.1.21;
RA Bergkessel M., Reese J.C.;
RT "An essential role for the Saccharomyces cerevisiae DEAD-box helicase DHH1
RT in G1/S DNA-damage checkpoint recovery.";
RL Genetics 167:21-33(2004).
RN [13]
RP FUNCTION.
RX PubMed=15703442; DOI=10.1261/rna.7258505;
RA Teixeira D., Sheth U., Valencia-Sanchez M.A., Brengues M., Parker R.;
RT "Processing bodies require RNA for assembly and contain nontranslating
RT mRNAs.";
RL RNA 11:371-382(2005).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15706350; DOI=10.1038/sj.emboj.7600560;
RA Muhlrad D., Parker R.;
RT "The yeast EDC1 mRNA undergoes deadenylation-independent decapping
RT stimulated by Not2p, Not4p, and Not5p.";
RL EMBO J. 24:1033-1045(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-425, AND MUTAGENESIS OF ARG-89;
RP LYS-91; ASP-195; GLU-196; ARG-345; GLY-346; HIS-369 AND ARG-370.
RX PubMed=15987810; DOI=10.1261/rna.2920905;
RA Cheng Z., Coller J.M., Parker R., Song H.;
RT "Crystal structure and functional analysis of DEAD-box protein Dhh1p.";
RL RNA 11:1258-1270(2005).
RN [17]
RP INTERACTION WITH IGO1.
RX PubMed=20471941; DOI=10.1016/j.molcel.2010.02.039;
RA Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S.,
RA Devgan G., Snyder M., Broach J.R., De Virgilio C.;
RT "Initiation of the TORC1-regulated G0 program requires Igo1/2, which
RT license specific mRNAs to evade degradation via the 5'-3' mRNA decay
RT pathway.";
RL Mol. Cell 38:345-355(2010).
RN [18]
RP FUNCTION, RNA-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=26098573; DOI=10.1038/ncb3189;
RA Hu G., McQuiston T., Bernard A., Park Y.D., Qiu J., Vural A., Zhang N.,
RA Waterman S.R., Blewett N.H., Myers T.G., Maraia R.J., Kehrl J.H., Uzel G.,
RA Klionsky D.J., Williamson P.R.;
RT "A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation
RT regulates autophagy.";
RL Nat. Cell Biol. 17:930-942(2015).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC more specifically in mRNA decapping by activating the decapping enzyme
CC DCP1 (PubMed:11780629, PubMed:12032091, PubMed:11696541,
CC PubMed:12730603, PubMed:15703442. PubMed:15706350). Is involved in G1/S
CC DNA-damage checkpoint recovery, probably through the regulation of the
CC translational status of a subset of mRNAs (PubMed:15166134). May also
CC have a role in translation and mRNA nuclear export (PubMed:12930949).
CC Required for sporulation (PubMed:12930949). Blocks autophagy in
CC nutrient-rich conditions by, at least partly, binding and repressing
CC the expression of a set of ATG genes, including ATG3, ATG7, ATG8,
CC ATG19, ATG20, ATG22 and SNX4/ATG24 (PubMed:26098573).
CC {ECO:0000269|PubMed:11696541, ECO:0000269|PubMed:11780629,
CC ECO:0000269|PubMed:12032091, ECO:0000269|PubMed:12730603,
CC ECO:0000269|PubMed:12930949, ECO:0000269|PubMed:15166134,
CC ECO:0000269|PubMed:15703442, ECO:0000269|PubMed:15706350,
CC ECO:0000269|PubMed:26098573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Associated with the CCR4-NOT complex and possibly other big
CC complexes (PubMed:9504907, PubMed:12930949). Interacts with CDC39/NOT1
CC (PubMed:11696541). Interacts with DCP1, LSM1, and POP2 (PubMed:9504907,
CC PubMed:11780629). Interacts with IGO1 (PubMed:20471941). Interacts with
CC PAT1 and with KEM1, the major 5'-3' exonuclease (PubMed:11780629,
CC PubMed:12032091). {ECO:0000269|PubMed:11696541,
CC ECO:0000269|PubMed:11780629, ECO:0000269|PubMed:12032091,
CC ECO:0000269|PubMed:12930949, ECO:0000269|PubMed:20471941,
CC ECO:0000269|PubMed:9504907}.
CC -!- INTERACTION:
CC P39517; Q12517: DCP1; NbExp=3; IntAct=EBI-158, EBI-38519;
CC P39517; P39998: EDC3; NbExp=3; IntAct=EBI-158, EBI-22300;
CC P39517; P47017: LSM1; NbExp=2; IntAct=EBI-158, EBI-174;
CC P39517; P38203: LSM2; NbExp=3; IntAct=EBI-158, EBI-180;
CC P39517; P40070: LSM4; NbExp=3; IntAct=EBI-158, EBI-188;
CC P39517; P39016: MPT5; NbExp=3; IntAct=EBI-158, EBI-2052996;
CC P39517; P25644: PAT1; NbExp=7; IntAct=EBI-158, EBI-204;
CC P39517; P39008: POP2; NbExp=3; IntAct=EBI-158, EBI-13629;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:12032091,
CC ECO:0000269|PubMed:12730603, ECO:0000269|PubMed:12930949,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15706350}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- DISRUPTION PHENOTYPE: Leads to an increased in autophagy flux
CC (PubMed:26098573). Causes an accumulation of ATG3, ATG7, ATG8, ATG19,
CC ATG20, ATG22 and SNX4/ATG24 transcripts in nutrient-replete conditions
CC (PubMed:26098573). {ECO:0000269|PubMed:26098573}.
CC -!- MISCELLANEOUS: Present with 42900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC subfamily. {ECO:0000305}.
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DR EMBL; X66057; CAA46853.1; -; Genomic_DNA.
DR EMBL; Z67750; CAA91586.1; -; Genomic_DNA.
DR EMBL; Z74208; CAA98734.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11700.1; -; Genomic_DNA.
DR PIR; S31229; S31229.
DR RefSeq; NP_010121.1; NM_001180220.1.
DR PDB; 1S2M; X-ray; 2.10 A; A=31-425.
DR PDB; 4BRU; X-ray; 3.24 A; A=46-422.
DR PDB; 4BRW; X-ray; 2.80 A; A=46-422.
DR PDBsum; 1S2M; -.
DR PDBsum; 4BRU; -.
DR PDBsum; 4BRW; -.
DR AlphaFoldDB; P39517; -.
DR SMR; P39517; -.
DR BioGRID; 31903; 3623.
DR DIP; DIP-1243N; -.
DR IntAct; P39517; 41.
DR MINT; P39517; -.
DR STRING; 4932.YDL160C; -.
DR iPTMnet; P39517; -.
DR MaxQB; P39517; -.
DR PaxDb; P39517; -.
DR PRIDE; P39517; -.
DR EnsemblFungi; YDL160C_mRNA; YDL160C; YDL160C.
DR GeneID; 851394; -.
DR KEGG; sce:YDL160C; -.
DR SGD; S000002319; DHH1.
DR VEuPathDB; FungiDB:YDL160C; -.
DR eggNOG; KOG0326; Eukaryota.
DR GeneTree; ENSGT00940000170366; -.
DR HOGENOM; CLU_003041_30_0_1; -.
DR InParanoid; P39517; -.
DR OMA; VCADEAP; -.
DR BioCyc; YEAST:G3O-29554-MON; -.
DR Reactome; R-SCE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR EvolutionaryTrace; P39517; -.
DR PRO; PR:P39517; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39517; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; ISS:SGD.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IMP:SGD.
DR GO; GO:0045900; P:negative regulation of translational elongation; IMP:SGD.
DR GO; GO:0033962; P:P-body assembly; IMP:SGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IDA:SGD.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA transport; Nucleotide-binding; Reference proteome; RNA-binding;
KW Translation regulation; Transport.
FT CHAIN 1..506
FT /note="ATP-dependent RNA helicase DHH1"
FT /id="PRO_0000055044"
FT DOMAIN 77..247
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 257..417
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..74
FT /note="Q motif"
FT MOTIF 195..198
FT /note="DEAD box"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 89
FT /note="R->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius; when associated with A-91. Impairs RNA
FT binding in vitro."
FT /evidence="ECO:0000269|PubMed:15987810"
FT MUTAGEN 91
FT /note="K->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius; when associated with A-89. Impairs RNA
FT binding in vitro."
FT /evidence="ECO:0000269|PubMed:15987810"
FT MUTAGEN 195
FT /note="D->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15987810"
FT MUTAGEN 196
FT /note="E->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15987810"
FT MUTAGEN 345
FT /note="R->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius. Impairs RNA binding in vitro."
FT /evidence="ECO:0000269|PubMed:15987810"
FT MUTAGEN 346
FT /note="G->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius. Impairs RNA binding in vitro."
FT /evidence="ECO:0000269|PubMed:15987810"
FT MUTAGEN 369
FT /note="H->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15987810"
FT MUTAGEN 370
FT /note="R->A: Leads to mRNA turnover defect and no growth at
FT 37 degrees Celsius. Impairs RNA binding in vitro."
FT /evidence="ECO:0000269|PubMed:15987810"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:1S2M"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:1S2M"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:1S2M"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4BRW"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:1S2M"
SQ SEQUENCE 506 AA; 57544 MW; 062CFA56DF6F2CEE CRC64;
MGSINNNFNT NNNSNTDLDR DWKTALNIPK KDTRPQTDDV LNTKGNTFED FYLKRELLMG
IFEAGFEKPS PIQEEAIPVA ITGRDILARA KNGTGKTAAF VIPTLEKVKP KLNKIQALIM
VPTRELALQT SQVVRTLGKH CGISCMVTTG GTNLRDDILR LNETVHILVG TPGRVLDLAS
RKVADLSDCS LFIMDEADKM LSRDFKTIIE QILSFLPPTH QSLLFSATFP LTVKEFMVKH
LHKPYEINLM EELTLKGITQ YYAFVEERQK LHCLNTLFSK LQINQAIIFC NSTNRVELLA
KKITDLGYSC YYSHARMKQQ ERNKVFHEFR QGKVRTLVCS DLLTRGIDIQ AVNVVINFDF
PKTAETYLHR IGRSGRFGHL GLAINLINWN DRFNLYKIEQ ELGTEIAAIP ATIDKSLYVA
ENDETVPVPF PIEQQSYHQQ AIPQQQLPSQ QQFAIPPQQH HPQFMVPPSH QQQQAYPPPQ
MPSQQGYPPQ QEHFMAMPPG QSQPQY
